An SCF-like ubiquitin ligase complex that controls presynaptic differentiation

Edward H. Liao, Wesley Hung, Benjamin Abrams and Mei Zhen ()
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Edward H. Liao: Samuel Lunenfeld Research Institute, University of Toronto
Wesley Hung: Samuel Lunenfeld Research Institute, University of Toronto
Benjamin Abrams: University of California
Mei Zhen: Samuel Lunenfeld Research Institute, University of Toronto

Nature, 2004, vol. 430, issue 6997, 345-350

Abstract: Abstract During synapse formation, specialized subcellular structures develop at synaptic junctions in a tightly regulated fashion. Cross-signalling initiated by ephrins, Wnts and transforming growth factor-β family members between presynaptic and postsynaptic termini are proposed to govern synapse formation1,2,3. It is not well understood how multiple signals are integrated and regulated by developing synaptic termini to control synaptic differentiation. Here we report the identification of FSN-1, a novel F-box protein that is required in presynaptic neurons for the restriction and/or maturation of synapses in Caenorhabditis elegans. Many F-box proteins are target recognition subunits of SCF (Skp, Cullin, F-box) ubiquitin-ligase complexes4,5,6,7. fsn-1 functions in the same pathway as rpm-1, a gene encoding a large protein with RING finger domains8,9. FSN-1 physically associates with RPM-1 and the C. elegans homologues of SKP1 and Cullin to form a new type of SCF complex at presynaptic periactive zones. We provide evidence that T10H9.2, which encodes the C. elegans receptor tyrosine kinase ALK (anaplastic lymphoma kinase10), may be a target or a downstream effector through which FSN-1 stabilizes synapse formation. This neuron-specific, SCF-like complex therefore provides a localized signal to attenuate presynaptic differentiation.

Date: 2004
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DOI: 10.1038/nature02647

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